HNRH3_HUMAN
ID HNRH3_HUMAN Reviewed; 346 AA.
AC P31942; A8K682; B3KRE1; Q9BSX1; Q9NP53; Q9NP96; Q9NPA7; Q9NPI4; Q9UFU4;
AC Q9Y4J5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H3;
DE Short=hnRNP H3;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein 2H9;
DE Short=hnRNP 2H9;
GN Name=HNRNPH3; Synonyms=HNRPH3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=8999868; DOI=10.1074/jbc.272.3.1827;
RA Mahe D., Mahl P., Gattoni R., Fischer N., Mattei M.-G., Stevenin J.,
RA Fuchs J.-P.;
RT "Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. Relation
RT with splicing and early heat shock-induced splicing arrest.";
RL J. Biol. Chem. 272:1827-1836(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RX PubMed=10858537; DOI=10.1016/s0167-4781(00)00092-0;
RA Honore B.;
RT "The hnRNP 2H9 gene, which is involved in the splicing reaction, is a
RT multiply spliced gene.";
RL Biochim. Biophys. Acta 1492:108-119(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-6; 56-76; 85-90; 98-104; 175-200; 223-253 AND
RP 262-323, ACETYLATION AT MET-1, METHYLATION AT ARG-287, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 56-67; 206-222; 233-253 AND 262-287, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 94-104 AND 288-298.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [10]
RP PROTEIN SEQUENCE OF 116-127, AND METHYLATION AT ARG-121.
RX PubMed=11152131; DOI=10.1110/ps.9.11.2210;
RA Yague J., Vazquez J., Lopez de Castro J.A.;
RT "A post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-
RT Arg, found in a natural HLA class I peptide ligand.";
RL Protein Sci. 9:2210-2217(2000).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-298 AND THR-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-298 AND THR-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; TYR-296 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-174; ARG-323 AND ARG-343,
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-116; ARG-121 AND ARG-129 (ISOFORM
RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-67, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in the splicing process and participates in early
CC heat shock-induced splicing arrest. Due to their great structural
CC variations the different isoforms may possess different functions in
CC the splicing reaction.
CC -!- INTERACTION:
CC P31942; P09651: HNRNPA1; NbExp=3; IntAct=EBI-711437, EBI-352662;
CC P31942-2; P61289: PSME3; NbExp=3; IntAct=EBI-16399628, EBI-355546;
CC P31942-2; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-16399628, EBI-25839575;
CC P31942-2; Q5T0L3: SPATA46; NbExp=3; IntAct=EBI-16399628, EBI-750105;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8999868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P31942-1; Sequence=Displayed;
CC Name=2; Synonyms=2H9A;
CC IsoId=P31942-2; Sequence=VSP_005840;
CC Name=3; Synonyms=2H9B;
CC IsoId=P31942-3; Sequence=VSP_005838;
CC Name=4; Synonyms=2H9C;
CC IsoId=P31942-4; Sequence=VSP_005839;
CC Name=5; Synonyms=2H9D;
CC IsoId=P31942-5; Sequence=VSP_005839, VSP_005843, VSP_005844;
CC Name=6; Synonyms=2H9E;
CC IsoId=P31942-6; Sequence=VSP_005841, VSP_005842, VSP_005843,
CC VSP_005844;
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DR EMBL; L32610; AAD45179.1; -; mRNA.
DR EMBL; AF132360; AAF68843.1; -; Genomic_DNA.
DR EMBL; AF132360; AAF68844.1; -; Genomic_DNA.
DR EMBL; AF132360; AAF68845.1; -; Genomic_DNA.
DR EMBL; AF132360; AAF68846.1; -; Genomic_DNA.
DR EMBL; AF132360; AAF68847.1; -; Genomic_DNA.
DR EMBL; AF132360; AAF68848.1; -; Genomic_DNA.
DR EMBL; AF132361; AAF68849.1; -; mRNA.
DR EMBL; AF132362; AAF68850.1; -; mRNA.
DR EMBL; AF132363; AAF68851.1; -; mRNA.
DR EMBL; AF132364; AAF68852.1; -; mRNA.
DR EMBL; AK091411; BAG52353.1; -; mRNA.
DR EMBL; AK291547; BAF84236.1; -; mRNA.
DR EMBL; AL117395; CAB55897.1; -; mRNA.
DR EMBL; CH471083; EAW54281.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54282.1; -; Genomic_DNA.
DR EMBL; BC004511; AAH04511.2; -; mRNA.
DR EMBL; BC039824; AAH39824.1; -; mRNA.
DR CCDS; CCDS7278.1; -. [P31942-1]
DR CCDS; CCDS7279.1; -. [P31942-2]
DR PIR; T17207; T17207.
DR RefSeq; NP_001309363.1; NM_001322434.1. [P31942-1]
DR RefSeq; NP_001309365.1; NM_001322436.1. [P31942-1]
DR RefSeq; NP_001309366.1; NM_001322437.1. [P31942-1]
DR RefSeq; NP_001309367.1; NM_001322438.1. [P31942-2]
DR RefSeq; NP_001309368.1; NM_001322439.1. [P31942-2]
DR RefSeq; NP_001309369.1; NM_001322440.1. [P31942-2]
DR RefSeq; NP_001309370.1; NM_001322441.1. [P31942-2]
DR RefSeq; NP_001309374.1; NM_001322445.1. [P31942-4]
DR RefSeq; NP_001309375.1; NM_001322446.1. [P31942-4]
DR RefSeq; NP_001309376.1; NM_001322447.1. [P31942-4]
DR RefSeq; NP_001309377.1; NM_001322448.1. [P31942-4]
DR RefSeq; NP_001309378.1; NM_001322449.1. [P31942-4]
DR RefSeq; NP_036339.1; NM_012207.2. [P31942-1]
DR RefSeq; NP_067676.2; NM_021644.3. [P31942-2]
DR RefSeq; XP_016871657.1; XM_017016168.1.
DR RefSeq; XP_016871658.1; XM_017016169.1.
DR AlphaFoldDB; P31942; -.
DR SMR; P31942; -.
DR BioGRID; 109430; 261.
DR IntAct; P31942; 105.
DR MINT; P31942; -.
DR STRING; 9606.ENSP00000265866; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P31942; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31942; -.
DR MetOSite; P31942; -.
DR PhosphoSitePlus; P31942; -.
DR SwissPalm; P31942; -.
DR BioMuta; HNRNPH3; -.
DR DMDM; 23503095; -.
DR EPD; P31942; -.
DR jPOST; P31942; -.
DR MassIVE; P31942; -.
DR MaxQB; P31942; -.
DR PaxDb; P31942; -.
DR PeptideAtlas; P31942; -.
DR PRIDE; P31942; -.
DR ProteomicsDB; 54808; -. [P31942-1]
DR ProteomicsDB; 54809; -. [P31942-2]
DR ProteomicsDB; 54810; -. [P31942-3]
DR ProteomicsDB; 54811; -. [P31942-4]
DR ProteomicsDB; 54812; -. [P31942-5]
DR ProteomicsDB; 54813; -. [P31942-6]
DR TopDownProteomics; P31942-1; -. [P31942-1]
DR TopDownProteomics; P31942-2; -. [P31942-2]
DR Antibodypedia; 14612; 105 antibodies from 23 providers.
DR DNASU; 3189; -.
DR Ensembl; ENST00000265866.12; ENSP00000265866.7; ENSG00000096746.18. [P31942-1]
DR Ensembl; ENST00000354695.5; ENSP00000346726.5; ENSG00000096746.18. [P31942-2]
DR GeneID; 3189; -.
DR KEGG; hsa:3189; -.
DR MANE-Select; ENST00000265866.12; ENSP00000265866.7; NM_012207.3; NP_036339.1.
DR UCSC; uc001jnw.5; human. [P31942-1]
DR CTD; 3189; -.
DR DisGeNET; 3189; -.
DR GeneCards; HNRNPH3; -.
DR HGNC; HGNC:5043; HNRNPH3.
DR HPA; ENSG00000096746; Low tissue specificity.
DR MIM; 602324; gene.
DR neXtProt; NX_P31942; -.
DR OpenTargets; ENSG00000096746; -.
DR PharmGKB; PA162391325; -.
DR VEuPathDB; HostDB:ENSG00000096746; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000157720; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; P31942; -.
DR OMA; HNMQHRY; -.
DR PhylomeDB; P31942; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; P31942; -.
DR SignaLink; P31942; -.
DR BioGRID-ORCS; 3189; 41 hits in 1091 CRISPR screens.
DR ChiTaRS; HNRNPH3; human.
DR GeneWiki; HNRPH3; -.
DR GenomeRNAi; 3189; -.
DR Pharos; P31942; Tbio.
DR PRO; PR:P31942; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P31942; protein.
DR Bgee; ENSG00000096746; Expressed in tendon of biceps brachii and 206 other tissues.
DR ExpressionAtlas; P31942; baseline and differential.
DR Genevisible; P31942; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR CDD; cd12732; RRM2_hnRNPH3; 1.
DR CDD; cd12735; RRM3_hnRNPH3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034970; hnRNPH3_RRM2.
DR InterPro; IPR034969; hnRNPH3_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..346
FT /note="Heterogeneous nuclear ribonucleoprotein H3"
FT /id="PRO_0000081861"
FT DOMAIN 16..93
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 195..270
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 121
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11152131"
FT MOD_RES 174
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 287
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 296
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 343
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10858537"
FT /id="VSP_005841"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10858537,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT /id="VSP_005839"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10858537"
FT /id="VSP_005838"
FT VAR_SEQ 132..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10858537,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_005840"
FT VAR_SEQ 138..145
FT /note="RGGDGYDG -> MCFSLNYT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10858537"
FT /id="VSP_005842"
FT VAR_SEQ 259..276
FT /note="QHRYIELFLNSTPGGGSG -> RKWCLWHTILFPKREFIK (in isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10858537"
FT /id="VSP_005843"
FT VAR_SEQ 277..346
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10858537"
FT /id="VSP_005844"
FT VARIANT 163
FT /note="N -> S (in dbSNP:rs2273903)"
FT /id="VAR_020333"
FT VARIANT 284
FT /note="G -> A (in dbSNP:rs16925347)"
FT /id="VAR_052226"
FT MOD_RES P31942-2:116
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P31942-2:121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P31942-2:129
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 346 AA; 36926 MW; F7D14C2947930E9E CRC64;
MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM DYQGRSTGEA
FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY DPPRRLLGQR PGPYDRPIGG
RGGYYGAGRG SMYDRMRRGG DGYDGGYGGF DDYGGYNNYG YGNDGFDDRM RDGRGMGGHG
YGGAGDASSG FHGGHFVHMR GLPFRATEND IANFFSPLNP IRVHIDIGAD GRATGEADVE
FVTHEDAVAA MSKDKNNMQH RYIELFLNST PGGGSGMGGS GMGGYGRDGM DNQGGYGSVG
RMGMGNNYSG GYGTPDGLGG YGRGGGGSGG YYGQGGMSGG GWRGMY
